byYounan, Nadine D.; Nadal, Rebecca C.; Davies, Paul; Brown, David R.; Viles, John H.
This article is from The Journal of Biological Chemistry , volume 287 . Abstract Background: Oxidation and protein misfolding are fundamental to prion diseases.Results: Oxidation generates a monomeric, helical, and molten globule followed by a β-conformation that lacks a cooperative fold.Conclusion: Oxidation of the prion protein destabilizes its native fold and shares a common misfolding pathway to amyloid fibers.Significance: The misfolding may explain the high levels of oxidized methionine... Source: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3436581
byWalsh, Keifer P.; Minamide, Laurie S.; Kane, Sarah J.; Shaw, Alisa E.; Brown, David R.; Pulford, Bruce; Zabel, Mark D.; Lambeth, J. David; Kuhn, Thomas B.; Bamburg, James R.
This article is from PLoS ONE , volume 9 . Abstract Neurites of neurons under acute or chronic stress form bundles of filaments (rods) containing 1∶1 cofilin∶actin, which impair transport and synaptic function. Rods contain disulfide cross-linked cofilin and are induced by treatments resulting in oxidative stress. Rods form rapidly (5–30 min) in >80% of cultured hippocampal or cortical neurons treated with excitotoxic levels of glutamate or energy depleted (hypoxia/ischemia or... Source: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3997518